While proanthocyanidins (PA) are effective in improving collagen's resistance to collagenolytic degradation, the direct incorporation of PA into an adhesive system is detrimental to the light-curing thereof. Conversely, the use of PA as a primer could circumvent this issue, but little is known about the efficacy of PA in stabilizing collagen when applied in a clinically relevant manner. This study investigated the pre- and post-digestion morphology of an acid-etched dentin collagen layer that underwent PA treatment for time periods on a scale of seconds. The null hypothesis, that there is no difference between the PA-treated and untreated control group, had to be rejected, since it was revealed that the untreated control could not survive 1 hr of exogenous collagenase digestion, while the PA-treated collagen could sustain at least 16 hrs of digestion with no perceptible changes in collagen structure. In addition, the stabilizing effect of the gold-standard cross-linker glutaraldehyde at comparable experimental conditions was found to be almost non-existent within the 5, 15, or 30 sec of cross-linking permitted. Therefore, PA have been proven to be extraordinarily efficient in stabilizing demineralized dentin collagen against enzymatic challenges in a clinically relevant setting, likely due to the non-covalent nature of their interaction with collagen molecules.
